Amino acid structures of multiple forms of amyloid-related serum protein SAA from a single individual

Multiple forms of the acute-phase serum protein SAA were isolated from the lipoprotein fraction of plasma from a single individual. These protein forms were purified by size-exclusion, ion-exchange, and reverse-phase high-pressure liquid chromatography, and then the tryptic peptides were subjected t...

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Bibliographic Details
Published in:Biochemistry (Easton) 1988-03, Vol.27 (5), p.1677-1682
Main Authors: Dwulet, Francis E, Wallace, David K, Benson, Merrill D
Format: Article
Language:English
Subjects:
Aged
Amino Acid Sequence
amyloid A protein
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Chromatography, Gel
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Fundamental and applied biological sciences. Psychology
Glycoproteins
Humans
Male
Molecular Sequence Data
Molecular Weight
Peptide Fragments - isolation & purification
plasma
Proteins
Serum Amyloid A Protein - isolation & purification
Trypsin
Waldenstrom Macroglobulinemia - blood
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Summary:Multiple forms of the acute-phase serum protein SAA were isolated from the lipoprotein fraction of plasma from a single individual. These protein forms were purified by size-exclusion, ion-exchange, and reverse-phase high-pressure liquid chromatography, and then the tryptic peptides were subjected to amino acid sequence analysis. A total of three distinct 104-residue proteins were identified. Two of these proteins differed only by having either an arginine or a histidine at position 71 while the third protein had seven amino acid differences. Each of these proteins has a 103-residue companion protein where the amino-terminal arginine has been removed. Two of these protein sequences match the two human SAA cDNA structures reported in the literature. The presence of three unique amino acid sequences in one individual is proof that there must be a minimum of two genes for SAA in humans.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00405a044